FKBP6_DROME
ID FKBP6_DROME Reviewed; 455 AA.
AC Q9W1I9;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Inactive peptidyl-prolyl cis-trans isomerase shutdown;
GN Name=shu; ORFNames=CG4735;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J., Champe M.,
RA Chavez C., Dorsett V., Farfan D., Frise E., George R., Gonzalez M.,
RA Guarin H., Li P., Liao G., Miranda A., Mungall C.J., Nunoo J., Pacleb J.,
RA Paragas V., Park S., Phouanenavong S., Wan K., Yu C., Lewis S.E.,
RA Rubin G.M., Celniker S.;
RL Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE,
RP AND MUTAGENESIS OF ALA-335.
RX PubMed=10978289; DOI=10.1093/genetics/156.1.245;
RA Munn K., Steward R.;
RT "The shut-down gene of Drosophila melanogaster encodes a novel FK506-
RT binding protein essential for the formation of germline cysts during
RT oogenesis.";
RL Genetics 156:245-256(2000).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND INTERACTION WITH
RP HSP83.
RX PubMed=22902557; DOI=10.1016/j.molcel.2012.07.021;
RA Olivieri D., Senti K.A., Subramanian S., Sachidanandam R., Brennecke J.;
RT "The cochaperone shutdown defines a group of biogenesis factors essential
RT for all piRNA populations in Drosophila.";
RL Mol. Cell 47:954-969(2012).
RN [6]
RP FUNCTION.
RX PubMed=22753781; DOI=10.1261/rna.034405.112;
RA Preall J.B., Czech B., Guzzardo P.M., Muerdter F., Hannon G.J.;
RT "shutdown is a component of the Drosophila piRNA biogenesis machinery.";
RL RNA 18:1446-1457(2012).
CC -!- FUNCTION: Co-chaperone required during oogenesis to repress
CC transposable elements and prevent their mobilization, which is
CC essential for the germline integrity. Acts via the piRNA metabolic
CC process, which mediates the repression of transposable elements during
CC meiosis by forming complexes composed of piRNAs and Piwi proteins and
CC govern the methylation and subsequent repression of transposons. Acts
CC as a co-chaperone via its interaction with Hsp83/HSP90 and is required
CC for the biogenesis of all three piRNA major populations.
CC {ECO:0000269|PubMed:10978289, ECO:0000269|PubMed:22753781,
CC ECO:0000269|PubMed:22902557}.
CC -!- SUBUNIT: Interacts with Hsp83. {ECO:0000269|PubMed:22902557}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10978289,
CC ECO:0000269|PubMed:22902557}. Note=Present in the cytoplasm of germ
CC cells. Component of the meiotic nuage, also named P granule, a germ-
CC cell-specific organelle required to repress transposon activity during
CC meiosis. Also present in Yb bodies.
CC -!- TISSUE SPECIFICITY: Strongly expressed in the germline stem cells and
CC in 16-cell cysts. Present in the germ cells throughout embryogenesis.
CC Defects are due to derepression of transposable elements and impaired
CC piRNA biogenesis. {ECO:0000269|PubMed:10978289}.
CC -!- DISRUPTION PHENOTYPE: Recessive female sterility with no effects on
CC zygotic viability. Some strong alleles (WQ41 and WM40) also lead to
CC male sterility. {ECO:0000269|PubMed:10978289,
CC ECO:0000269|PubMed:22902557}.
CC -!- SIMILARITY: Belongs to the FKBP6 family. {ECO:0000305}.
CC -!- CAUTION: Although it contains a PPIase FKBP-type domain, does not show
CC peptidyl-prolyl cis-trans isomerase activity. {ECO:0000305}.
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DR EMBL; AE013599; AAF47070.1; -; Genomic_DNA.
DR EMBL; AY058554; AAL13783.1; -; mRNA.
DR RefSeq; NP_611837.1; NM_137993.4.
DR AlphaFoldDB; Q9W1I9; -.
DR SMR; Q9W1I9; -.
DR BioGRID; 69621; 7.
DR IntAct; Q9W1I9; 2.
DR STRING; 7227.FBpp0072146; -.
DR PaxDb; Q9W1I9; -.
DR PRIDE; Q9W1I9; -.
DR DNASU; 45360; -.
DR EnsemblMetazoa; FBtr0072237; FBpp0072146; FBgn0003401.
DR GeneID; 45360; -.
DR KEGG; dme:Dmel_CG4735; -.
DR UCSC; CG4735-RA; d. melanogaster.
DR CTD; 45360; -.
DR FlyBase; FBgn0003401; shu.
DR VEuPathDB; VectorBase:FBgn0003401; -.
DR eggNOG; KOG0543; Eukaryota.
DR GeneTree; ENSGT00940000158514; -.
DR HOGENOM; CLU_013615_13_2_1; -.
DR InParanoid; Q9W1I9; -.
DR OMA; GCPPRIK; -.
DR OrthoDB; 1465346at2759; -.
DR PhylomeDB; Q9W1I9; -.
DR BioGRID-ORCS; 45360; 0 hits in 1 CRISPR screen.
DR ChiTaRS; para; fly.
DR GenomeRNAi; 45360; -.
DR PRO; PR:Q9W1I9; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0003401; Expressed in secondary oocyte and 19 other tissues.
DR Genevisible; Q9W1I9; DM.
DR GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR GO; GO:0043186; C:P granule; IDA:FlyBase.
DR GO; GO:0070725; C:Yb body; IDA:FlyBase.
DR GO; GO:0051879; F:Hsp90 protein binding; IBA:GO_Central.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:InterPro.
DR GO; GO:0031047; P:gene silencing by RNA; IEA:UniProtKB-KW.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0048477; P:oogenesis; IMP:FlyBase.
DR GO; GO:0034587; P:piRNA metabolic process; IMP:FlyBase.
DR GO; GO:0007283; P:spermatogenesis; IBA:GO_Central.
DR Gene3D; 1.25.40.10; -; 1.
DR Gene3D; 3.10.50.40; -; 1.
DR InterPro; IPR042282; FKBP6/shu.
DR InterPro; IPR046357; PPIase_dom_sf.
DR InterPro; IPR001179; PPIase_FKBP_dom.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR46674; PTHR46674; 1.
DR Pfam; PF00254; FKBP_C; 1.
DR SUPFAM; SSF48452; SSF48452; 1.
DR PROSITE; PS50059; FKBP_PPIASE; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Differentiation; Meiosis; Oogenesis; Reference proteome; Repeat;
KW RNA-mediated gene silencing; TPR repeat.
FT CHAIN 1..455
FT /note="Inactive peptidyl-prolyl cis-trans isomerase
FT shutdown"
FT /id="PRO_0000428729"
FT DOMAIN 103..192
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00277"
FT REPEAT 218..251
FT /note="TPR 1"
FT REPEAT 303..336
FT /note="TPR 2"
FT REGION 34..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 335
FT /note="A->T: In PB70; weak allele that only affects female
FT fertility without affecting male fertility."
FT /evidence="ECO:0000269|PubMed:10978289"
SQ SEQUENCE 455 AA; 51838 MW; 45F1ED2FBEC61749 CRC64;
MEENFEPYTP QLLKNPLSYS DLVKKGVEFE VDNSQQNHAR DLGLDSDSDS DYEDALDVDG
EELRSPWTYS FDELRALMSE IDENIYKRIT RTGHVDREAV PNKARVSVRY SGYWEGETAP
FDSSLLRGSK FVFETGQGTV VEGLEVAVRS MRPYEQAEFI ISYKLLFGEL GCPPRIKPKA
DALFKVEVID YSLIGDAKGI DAIPQEDRDK FCVVYPKAVD LHLHGKDSVK LGRYQSAATA
FERAVSSLNY CRMANDEEER KQTELLTTLN QNLMIVYNKM NKPKRACIMM KALRHLTMGN
PSCKALFQEG RALAALGEYN LARNAYLQAQ AKQPANKEIS DEIISMNKRI SKYEEASRDI
WARAFSLKNS KSDVRKTPAQ LEKEAKEQDF NDKMEDLIRR FKNTSDQQVS FSRKSYSNAQ
FDATCKLAKE HNLKLTLSPI QEDVLTLSKP DVKFA
